1tdr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tdr.jpg|left|200px]]<br /><applet load="1tdr" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1tdr.jpg|left|200px]]
-
caption="1tdr, resolution 2.5&Aring;" />
+
 
-
'''EXPRESSION, CHARACTERIZATION, AND CRYSTALLOGRAPHIC ANALYSIS OF TELLUROMETHIONYL DIHYDROFOLATE REDUCTASE'''<br />
+
{{Structure
 +
|PDB= 1tdr |SIZE=350|CAPTION= <scene name='initialview01'>1tdr</scene>, resolution 2.5&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MTX:METHOTREXATE'>MTX</scene> and <scene name='pdbligand=TE:TELLURIUM'>TE</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3]
 +
|GENE=
 +
}}
 +
 
 +
'''EXPRESSION, CHARACTERIZATION, AND CRYSTALLOGRAPHIC ANALYSIS OF TELLUROMETHIONYL DIHYDROFOLATE REDUCTASE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1TDR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MTX:'>MTX</scene> and <scene name='pdbligand=TE:'>TE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDR OCA].
+
1TDR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDR OCA].
==Reference==
==Reference==
-
Expression, characterization and crystallographic analysis of telluromethionyl dihydrofolate reductase., Boles JO, Lewinski K, Kunckle MG, Hatada M, Lebioda L, Dunlap RB, Odom JD, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):731-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299803 15299803]
+
Expression, characterization and crystallographic analysis of telluromethionyl dihydrofolate reductase., Boles JO, Lewinski K, Kunckle MG, Hatada M, Lebioda L, Dunlap RB, Odom JD, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):731-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299803 15299803]
[[Category: Dihydrofolate reductase]]
[[Category: Dihydrofolate reductase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
Line 22: Line 31:
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:33 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:03 2008''

Revision as of 12:17, 20 March 2008

Image:1tdr.jpg


PDB ID 1tdr

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , and
Activity: Dihydrofolate reductase, with EC number 1.5.1.3
Coordinates: save as pdb, mmCIF, xml



EXPRESSION, CHARACTERIZATION, AND CRYSTALLOGRAPHIC ANALYSIS OF TELLUROMETHIONYL DIHYDROFOLATE REDUCTASE


Overview

Selenomethionine-containing proteins analyzed by multi-wavelength anomalous diffraction provide a facile means of addressing the phase problem, whose solution is necessary to determine protein structures by X-ray crystallography [Hendrickson (1991). Science, 254, 51-58]. Since this method requires synchrotron radiation, we sought to incorporate a true heavy atom into protein, allowing the solution of the phase problem by more traditional methods of data collection. Media containing TeMet alone or TeMet with low levels of Met failed to sustain growth of a methione auxotroph of Escherichia coli carrying the dihydrofolate reductase expression vector. Growth of the organism to stationary phase and incorporation of TeMet was observed when the culture was initiated in media containing minimal Met levels and TeMet was added after induction with isopropyl-1-thio-beta-D-galactopyranoside. The purified enzyme exhibited properties similar to those of the native enzyme. Atomic absorption spectroscopy and amino-acid analysis indicated that 40% of the methionines were replaced with TeMet. Sequence analysis did not indicate significant levels of replacement in the first three sites (1, 16 and 20), suggesting that TeMet was present only in the last two sites (42 and 92). Crystals of this enzyme were grown in the presence of methotrexate and were isomorphous with crystals of wild-type dihydrofolate reductase. Difference Fourier maps and restrained least-squares refinement showed no substitution at the first three methionines, while incorporation was seen at positions 42 and 92.

About this Structure

1TDR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Expression, characterization and crystallographic analysis of telluromethionyl dihydrofolate reductase., Boles JO, Lewinski K, Kunckle MG, Hatada M, Lebioda L, Dunlap RB, Odom JD, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):731-9. PMID:15299803

Page seeded by OCA on Thu Mar 20 14:17:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tdr"
Personal tools